p(HBP:"6D tau", frag("2_18"))

Entity

Name

6D tau

Namespace

HBP

Namespace Version

None

Pattern

.*

Again, coperfusion of the PAD peptide with either I-2 (50 nM) (Fig. 5A) or ING-135 (100 nM) (Fig. 5B) anterograde FAT inhibition. PubMed:21734277

Again, coperfusion of the PAD peptide with either I-2 (50 nM) (Fig. 5A) or ING-135 (100 nM) (Fig. 5B) anterograde FAT inhibition. PubMed:21734277

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

Together, these data suggest that increased PAD exposure represents an early event in AD pathogenesis and that AT8 may not be required for PAD ex- posure in situ. PubMed:21734277

To evaluate the relevance of these find- ings in human disease, we generated a novel monoclonal antibody, termed TNT1, which specifically recognizes PAD. PubMed:21734277

These data indicated that increased PAD exposure, as revealed by TNT1 immunoreac- tivity, occurs early in AD and remains present throughout the disease process. PubMed:21734277

Together, these data suggest that increased PAD exposure represents an early event in AD pathogenesis and that AT8 may not be required for PAD ex- posure in situ. PubMed:21734277

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

As observed with 􏰁2–18 tau aggregates (LaPointe et al., 2009), monomeric 􏰁2–18 6D tau showed no effect on FAT (Fig. 4 A, D), demonstrating that PAD is necessary for 6D tau- mediated inhibition of anterograde FAT. PubMed:21734277

The PAD peptide selectively in- hibited anterograde FAT (Fig. 4 B, D), but not retrograde FAT (Fig. 4B,E). PubMed:21734277

Collectively, these data indicate that PAD is both necessary and sufficient to inhibit an- terograde FAT by activating the PP1–GSK3 cascade. PubMed:21734277

The PAD peptide selectively in- hibited anterograde FAT (Fig. 4 B, D), but not retrograde FAT (Fig. 4B,E). PubMed:21734277

P-c-Jun was dephosphorylated to a greater extent in PAD peptide-perfused axoplasms than their scrambled peptide- perfused counterpart (Fig. 5F ), suggesting that the PAD peptide induced activation of endogenous axoplasmic phosphatases. PubMed:21734277

A trend of elevated GSK3 activity (􏰈32%) relative to PKC activity ( p 􏰄 0.28, paired t test; n 􏰄 3) was observed for axoplasms incubated with the PAD peptide (mean 􏰄 4.9 􏰉 2.5), compared with those incubated with scram- bled peptide (mean 􏰄 3.7 􏰉 1.7), which supports the results from vesicle motility assays. PubMed:21734277

Collectively, these data indicate that PAD is both necessary and sufficient to inhibit an- terograde FAT by activating the PP1–GSK3 cascade. PubMed:21734277

To evaluate the relevance of these find- ings in human disease, we generated a novel monoclonal antibody, termed TNT1, which specifically recognizes PAD. PubMed:21734277

These data indicated that increased PAD exposure, as revealed by TNT1 immunoreac- tivity, occurs early in AD and remains present throughout the disease process. PubMed:21734277

Together, these data suggest that increased PAD exposure represents an early event in AD pathogenesis and that AT8 may not be required for PAD ex- posure in situ. PubMed:21734277